Purification of the peptidoglycan transglycosylase of Bacillus megaterium.
The peptidoglycan transglycosylase of Bacillus megaterium has been purified approximately 500-fold from a crude membrane fraction. This protein is likely to be the one previously called PG-II and was assayed by its ability to reconstitute with a crude phospho-N-acetyl-muramyl-pentapeptide translocase preparation and partially purified N-acetylglucosaminyl transferase to give peptidoglycan synthesis from nucleotide precursors. The protein was identified as the peptidoglycan transglycosylase by its ability to synthesize lysozyme-sensitive peptidoglycan from undecaprenylpyrophosphoryl-disaccharide-pentapeptide. The enzyme is inhibited by vancomycin but not by bacitracin, penicillin G, or tunicamycin. The enzyme has no detectable transpeptidase activity, but it does bind penicillin.
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001410:Bacillus megaterium / Q000201:enzymology*; D006602:Hexosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D046928:Peptidoglycan Glycosyltransferase; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D013439:Sulfhydryl Reagents; D006602:Hexosyltransferases; D046928:Peptidoglycan Glycosyltransferase